ID ZRAN1_XENTR Reviewed; 701 AA. AC B1H2Q2; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Ubiquitin thioesterase zranb1 {ECO:0000305}; DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9UGI0}; DE AltName: Full=Zinc finger Ran-binding domain-containing protein 1; GN Name=zranb1; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys- CC 29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also CC cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency CC compared to 'Lys-29'-linked ones (By similarity). Positive regulator of CC the Wnt signaling pathway that deubiquitinates apc protein, a negative CC regulator of Wnt-mediated transcription (By similarity). Acts as a CC regulator of autophagy by mediating deubiquitination of pik3c3/vps34, CC thereby promoting autophagosome maturation (By similarity). Plays a CC role in the regulation of cell morphology and cytoskeletal organization CC (By similarity). Required in the stress fiber dynamics and cell CC migration (By similarity). {ECO:0000250|UniProtKB:Q9UGI0}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9UGI0}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UGI0}. Nucleus CC {ECO:0000250|UniProtKB:Q9UGI0}. Note=Enriched in punctate localization CC in the cytoplasm. {ECO:0000250|UniProtKB:Q9UGI0}. CC -!- DOMAIN: The RanBP2-type zinc fingers, also called NZFs, mediate the CC interaction with ubiquitin and determine linkage specificity. RanBP2- CC type zinc fingers 1 and 2 (also named NZF1 and NZF2) specifically CC recognize and bind 'Lys-29'- and 'Lys-33'-linked ubiquitin. RanBP2-type CC zinc finger 3 (also named NZF3) binds 'Lys-33'-linked ubiquitin and CC shows weak binding to 'Lys-6'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin CC chains but it does not interact with 'Lys-29'-linked chains. CC {ECO:0000250|UniProtKB:Q9UGI0}. CC -!- DOMAIN: The OTU domain mediates the deubiquitinating activity. CC {ECO:0000250|UniProtKB:Q9UGI0}. CC -!- DOMAIN: The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts CC with ubiquitin hydrophobic patch and contributes to linkage CC specificity. {ECO:0000250|UniProtKB:Q9UGI0}. CC -!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC161086; AAI61086.1; -; mRNA. DR RefSeq; NP_001116900.1; NM_001123428.1. DR AlphaFoldDB; B1H2Q2; -. DR SMR; B1H2Q2; -. DR STRING; 8364.ENSXETP00000040428; -. DR MEROPS; C64.004; -. DR PaxDb; 8364-ENSXETP00000050986; -. DR GeneID; 100144659; -. DR KEGG; xtr:100144659; -. DR AGR; Xenbase:XB-GENE-876399; -. DR CTD; 54764; -. DR Xenbase; XB-GENE-876399; zranb1. DR eggNOG; KOG4345; Eukaryota. DR InParanoid; B1H2Q2; -. DR OrthoDB; 2909231at2759; -. DR Proteomes; UP000008143; Chromosome 7. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016477; P:cell migration; ISS:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB. DR GO; GO:0035523; P:protein K29-linked deubiquitination; ISS:UniProtKB. DR GO; GO:1990168; P:protein K33-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd22767; OTU_ZRANB1; 1. DR Gene3D; 1.25.40.560; -; 1. DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3. DR InterPro; IPR041294; AnkUBD. DR InterPro; IPR003323; OTU_dom. DR InterPro; IPR001876; Znf_RanBP2. DR InterPro; IPR036443; Znf_RanBP2_sf. DR InterPro; IPR049768; ZRANB1_OTU. DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1. DR PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1. DR Pfam; PF18418; AnkUBD; 1. DR Pfam; PF02338; OTU; 1. DR Pfam; PF00641; zf-RanBP; 2. DR SMART; SM00547; ZnF_RBZ; 3. DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2. DR PROSITE; PS50802; OTU; 1. DR PROSITE; PS01358; ZF_RANBP2_1; 3. DR PROSITE; PS50199; ZF_RANBP2_2; 3. PE 2: Evidence at transcript level; KW ANK repeat; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Protease; KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway; KW Wnt signaling pathway; Zinc; Zinc-finger. FT CHAIN 1..701 FT /note="Ubiquitin thioesterase zranb1" FT /id="PRO_0000361558" FT REPEAT 253..283 FT /note="ANK 1" FT REPEAT 306..333 FT /note="ANK 2" FT DOMAIN 425..585 FT /note="OTU" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139" FT ZN_FING 3..33 FT /note="RanBP2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT ZN_FING 79..108 FT /note="RanBP2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT ZN_FING 143..173 FT /note="RanBP2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT REGION 38..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 108..129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 198..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 108..124 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 198..212 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 436 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q9UGI0" FT ACT_SITE 578 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q6GQQ9" FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 164 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" SQ SEQUENCE 701 AA; 80037 MW; DD3A68A82AF3DADE CRC64; MTEHGIKWAC EYCTYENWPS AIKCTMCRAP RPSGAIITEE PFKNSTPDVG SMERESGSPL ICPDSSARPR VKSSYSMETS TKWSCHMCTY LNWPRAIRCT QCLSQRRTRS PTESPQSSGS SLRAIPSPID PCEEYNDRNK LNIKGQHWTC SACTYENCAK AKKCVVCDHP TPNNMDAIEL ANTDEASSII NEQDRARWRG GCSSSNSQRR SPPTSKRDSD MDFQRIELAG AVGSKEEFEL DLKKLKQIKN RMRKTDWLFL NACVGVVEGD LSAVEAYKTS GGDIARQLSA DEVRLLNRPS AFDVGYTLVH LSIRFQRQDM LAILLTEFSQ HAAKCIPAMV CPELTEQIRR EIAASVHQRK GDFACYFLTD LVTFTLPADI EDLPPTVQEK LFDEVLDRDV QKELEEESPI INWSLELGTR LDSRLYALWN RTAGDCLLDS VLQATWGIYD KDSVLRKALH DSLHDCSHWF YSRWKEWESW YSQSFGLHFS LREEQWQEDW AFILSLASQP GASLEQTHIF VLAHILRRPI IVYGVKYYKS FRGETLGYTR FQGVYLPLLW EQSFCWKSPI ALGYTRGHFS ALVAMENDGF DNRGAGANLN TDDDVTVTFL PLVDSERKLL HIHFLSAQEL GNEDQQEKLL REWMDCCVTE GGVLVAMQKS SRRRNHPLVT QMVEKWLDGY RQIRPCTALS DGEEDEDDED E //